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PDBsum entry 2ln0
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References listed in PDB file
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Key reference
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Title
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Combinatorial readout of unmodified h3r2 and acetylated h3k14 by the tandem phd finger of moz reveals a regulatory mechanism for hoxa9 transcription.
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Authors
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Y.Qiu,
L.Liu,
C.Zhao,
C.Han,
F.Li,
J.Zhang,
Y.Wang,
G.Li,
Y.Mei,
M.Wu,
J.Wu,
Y.Shi.
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Ref.
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Genes Dev, 2012,
26,
1376-1391.
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PubMed id
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Abstract
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Histone acetylation is a hallmark for gene transcription. As a histone
acetyltransferase, MOZ (monocytic leukemia zinc finger protein) is important for
HOX gene expression as well as embryo and postnatal development. In vivo, MOZ
forms a tetrameric complex with other subunits, including several
chromatin-binding modules with regulatory functions. Here we report the solution
structure of the tandem PHD (plant homeodomain) finger (PHD12) of human MOZ in a
free state and the 1.47 Å crystal structure in complex with H3K14ac peptide,
which reveals the structural basis for the recognition of unmodified R2 and
acetylated K14 on histone H3. Moreover, the results of chromatin
immunoprecipitation (ChIP) and RT-PCR assays indicate that PHD12 facilitates the
localization of MOZ onto the promoter locus of the HOXA9 gene, thereby promoting
the H3 acetylation around the promoter region and further up-regulating the
HOXA9 mRNA level. Taken together, our findings suggest that the combinatorial
readout of the H3R2/K14ac by PHD12 might represent an important epigenetic
regulatory mechanism that governs transcription and also provide a clue of
cross-talk between the MOZ complex and histone H3 modifications.
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